The Nesprin Family Member ANC-1 Regulates Synapse Formation and Axon Termination by Functioning in a Pathway with RPM-1 and β-Catenin
Figure 1
(A) Schematic of ANC-1 protein structure which consists of two calponin homology (CH) domains that bind F-actin (dashed boxes), 6 repeat regions (grey), and a KASH domain (black) that mediates binding to the nucleus. Also shown is the C-terminal domain of ANC-1 that functions as a dominant negative. (B) CoIP of endogenous ANC-1 with RPM-1::GFP. CoIPs were performed from whole worm lysates prepared from transgenic animals (juIs58) or non-transgenic animals (N2). (C) Epifluorescent microscopy was used to visualize SUR-5::GFP in the multinucleated hypodermal cells of C. elegans. In wild-type animals, nuclei are anchored to the actin cytoskeleton and evenly spaced throughout the syncytium (arrowheads). In anc-1 mutants, impaired nuclear anchorage leads to aggregation of nuclei (arrows). Scale bar is 20 µm.